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P35556

- FBN2_HUMAN

UniProt

P35556 - FBN2_HUMAN

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Protein

Fibrillin-2

Gene

FBN2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Fibrillins are structural components of 10-12 nm extracellular calcium-binding microfibrils, which occur either in association with elastin or in elastin-free bundles. Fibrillin-2-containing microfibrils regulate the early process of elastic fiber assembly. Regulates osteoblast maturation by controlling TGF-beta bioavailability and calibrating TGF-beta and BMP levels, respectively By similarity.By similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. extracellular matrix structural constituent Source: ProtInc

GO - Biological processi

  1. anatomical structure morphogenesis Source: ProtInc
  2. bone trabecula formation Source: BHF-UCL
  3. embryonic limb morphogenesis Source: Ensembl
  4. extracellular matrix disassembly Source: Reactome
  5. extracellular matrix organization Source: Reactome
  6. positive regulation of bone mineralization Source: BHF-UCL
  7. positive regulation of osteoblast differentiation Source: BHF-UCL
  8. sequestering of TGFbeta in extracellular matrix Source: BHF-UCL
Complete GO annotation...

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_150331. Molecules associated with elastic fibres.
REACT_150366. Elastic fibre formation.

Names & Taxonomyi

Protein namesi
Recommended name:
Fibrillin-2
Gene namesi
Name:FBN2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:3604. FBN2.

Subcellular locationi

GO - Cellular componenti

  1. extracellular matrix Source: UniProtKB
  2. extracellular region Source: Reactome
  3. microfibril Source: BHF-UCL
  4. proteinaceous extracellular matrix Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Arthrogryposis, distal, 9 (DA9) [MIM:121050]: A form of distal arthrogryposis, a disease characterized by congenital joint contractures that mainly involve two or more distal parts of the limbs, in the absence of a primary neurological or muscle disease. DA9 is a connective tissue disorder characterized by contractures, arachnodactyly, scoliosis, and crumpled ears.6 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti391 – 3911E → K in DA9.
VAR_015851
Natural varianti754 – 7541G → S in DA9. 1 Publication
VAR_058364
Natural varianti1057 – 10571G → D in DA9. 2 Publications
VAR_054981
Natural varianti1091 – 10911N → S in DA9. 1 Publication
VAR_058365
Natural varianti1093 – 10931I → T in DA9. 2 Publications
VAR_054982
Natural varianti1115 – 11151D → H in DA9; the underlying nucleotide substitution also causes low level in-frame mis-splicing of exon 25. 2 Publications
VAR_010739
Natural varianti1122 – 11221S → P in DA9. 1 Publication
VAR_058366
Natural varianti1142 – 11421C → F in DA9. 2 Publications
VAR_010740
Natural varianti1142 – 11421C → R in DA9. 1 Publication
VAR_058367
Natural varianti1146 – 11461Y → C in DA9. 1 Publication
VAR_058368
Natural varianti1156 – 11561C → F in DA9. 1 Publication
VAR_058369
Natural varianti1161 – 11611E → K in DA9. 1 Publication
VAR_058370
Natural varianti1179 – 11791G → C in DA9. 1 Publication
VAR_054983
Natural varianti1198 – 11981C → Y in DA9. 1 Publication
VAR_054984
Natural varianti1240 – 12401C → R in DA9. 1 Publication
VAR_054985
Natural varianti1246 – 12461C → F in DA9. 1 Publication
VAR_058371
Natural varianti1253 – 12531C → W in DA9. 2 Publications
Corresponds to variant rs28931602 [ dbSNP | Ensembl ].
VAR_010741
Natural varianti1253 – 12531C → Y in DA9. 2 Publications
VAR_002350
Natural varianti1257 – 12571C → W in DA9. 1 Publication
VAR_054986
Natural varianti1268 – 12681C → R in DA9. 1 Publication
VAR_054987
Natural varianti1384 – 13841C → F in DA9. 1 Publication
VAR_058372
Natural varianti1384 – 13841C → Y in DA9. 1 Publication
VAR_058373
Natural varianti1408 – 14081D → N in DA9. 1 Publication
VAR_058374
Natural varianti1425 – 14251C → R in DA9. 1 Publication
VAR_058375
Natural varianti1434 – 14341C → S in DA9. 2 Publications
VAR_002351

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi121050. phenotype.
Orphaneti115. Congenital contractural arachnodactyly.
PharmGKBiPA28017.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence AnalysisAdd
BLAST
Chaini29 – 29122884Fibrillin-2PRO_0000007584Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi115 ↔ 124PROSITE-ProRule annotation
Disulfide bondi119 ↔ 130PROSITE-ProRule annotation
Disulfide bondi132 ↔ 141PROSITE-ProRule annotation
Disulfide bondi149 ↔ 159PROSITE-ProRule annotation
Disulfide bondi153 ↔ 164PROSITE-ProRule annotation
Disulfide bondi166 ↔ 175PROSITE-ProRule annotation
Disulfide bondi180 ↔ 190PROSITE-ProRule annotation
Disulfide bondi184 ↔ 196PROSITE-ProRule annotation
Disulfide bondi198 ↔ 207PROSITE-ProRule annotation
Disulfide bondi280 ↔ 292PROSITE-ProRule annotation
Disulfide bondi287 ↔ 301PROSITE-ProRule annotation
Disulfide bondi303 ↔ 316PROSITE-ProRule annotation
Disulfide bondi322 ↔ 334PROSITE-ProRule annotation
Disulfide bondi329 ↔ 343PROSITE-ProRule annotation
Disulfide bondi345 ↔ 358PROSITE-ProRule annotation
Glycosylationi492 – 4921N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi498 ↔ 510PROSITE-ProRule annotation
Disulfide bondi505 ↔ 519PROSITE-ProRule annotation
Disulfide bondi521 ↔ 533PROSITE-ProRule annotation
Disulfide bondi539 ↔ 549PROSITE-ProRule annotation
Disulfide bondi544 ↔ 558PROSITE-ProRule annotation
Disulfide bondi560 ↔ 573PROSITE-ProRule annotation
Disulfide bondi579 ↔ 591PROSITE-ProRule annotation
Disulfide bondi586 ↔ 600PROSITE-ProRule annotation
Disulfide bondi602 ↔ 615PROSITE-ProRule annotation
Disulfide bondi621 ↔ 632PROSITE-ProRule annotation
Disulfide bondi627 ↔ 641PROSITE-ProRule annotation
Disulfide bondi643 ↔ 656PROSITE-ProRule annotation
Disulfide bondi662 ↔ 673PROSITE-ProRule annotation
Disulfide bondi668 ↔ 682PROSITE-ProRule annotation
Disulfide bondi684 ↔ 697PROSITE-ProRule annotation
Disulfide bondi772 ↔ 784PROSITE-ProRule annotation
Disulfide bondi779 ↔ 793PROSITE-ProRule annotation
Disulfide bondi795 ↔ 808PROSITE-ProRule annotation
Disulfide bondi814 ↔ 826PROSITE-ProRule annotation
Disulfide bondi821 ↔ 835PROSITE-ProRule annotation
Disulfide bondi837 ↔ 850PROSITE-ProRule annotation
Disulfide bondi856 ↔ 866PROSITE-ProRule annotation
Disulfide bondi861 ↔ 875PROSITE-ProRule annotation
Disulfide bondi877 ↔ 890PROSITE-ProRule annotation
Disulfide bondi959 ↔ 971PROSITE-ProRule annotation
Disulfide bondi966 ↔ 980PROSITE-ProRule annotation
Disulfide bondi982 ↔ 995PROSITE-ProRule annotation
Disulfide bondi1077 ↔ 1089PROSITE-ProRule annotation
Disulfide bondi1084 ↔ 1098PROSITE-ProRule annotation
Disulfide bondi1100 ↔ 1113PROSITE-ProRule annotation
Glycosylationi1112 – 11121N-linked (GlcNAc...)1 Publication
Disulfide bondi1119 ↔ 1131PROSITE-ProRule annotation
Disulfide bondi1126 ↔ 1140PROSITE-ProRule annotation
Disulfide bondi1142 ↔ 1156PROSITE-ProRule annotation
Disulfide bondi1162 ↔ 1174PROSITE-ProRule annotation
Disulfide bondi1169 ↔ 1183PROSITE-ProRule annotation
Disulfide bondi1185 ↔ 1198PROSITE-ProRule annotation
Disulfide bondi1204 ↔ 1216PROSITE-ProRule annotation
Disulfide bondi1211 ↔ 1225PROSITE-ProRule annotation
Disulfide bondi1227 ↔ 1240PROSITE-ProRule annotation
Disulfide bondi1246 ↔ 1257PROSITE-ProRule annotation
Disulfide bondi1253 ↔ 1266PROSITE-ProRule annotation
Disulfide bondi1268 ↔ 1281PROSITE-ProRule annotation
Disulfide bondi1287 ↔ 1299PROSITE-ProRule annotation
Disulfide bondi1294 ↔ 1308PROSITE-ProRule annotation
Disulfide bondi1310 ↔ 1323PROSITE-ProRule annotation
Disulfide bondi1329 ↔ 1341PROSITE-ProRule annotation
Disulfide bondi1336 ↔ 1350PROSITE-ProRule annotation
Disulfide bondi1352 ↔ 1365PROSITE-ProRule annotation
Disulfide bondi1371 ↔ 1384PROSITE-ProRule annotation
Disulfide bondi1378 ↔ 1393PROSITE-ProRule annotation
Disulfide bondi1395 ↔ 1406PROSITE-ProRule annotation
Disulfide bondi1412 ↔ 1425PROSITE-ProRule annotation
Glycosylationi1414 – 14141N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1419 ↔ 1434PROSITE-ProRule annotation
Disulfide bondi1436 ↔ 1447PROSITE-ProRule annotation
Disulfide bondi1453 ↔ 1465PROSITE-ProRule annotation
Disulfide bondi1460 ↔ 1474PROSITE-ProRule annotation
Disulfide bondi1476 ↔ 1489PROSITE-ProRule annotation
Disulfide bondi1495 ↔ 1506PROSITE-ProRule annotation
Disulfide bondi1501 ↔ 1515PROSITE-ProRule annotation
Disulfide bondi1517 ↔ 1530PROSITE-ProRule annotation
Glycosylationi1529 – 15291N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1536 ↔ 1547PROSITE-ProRule annotation
Disulfide bondi1542 ↔ 1556PROSITE-ProRule annotation
Disulfide bondi1558 ↔ 1571PROSITE-ProRule annotation
Glycosylationi1625 – 16251N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1654 ↔ 1666PROSITE-ProRule annotation
Disulfide bondi1661 ↔ 1675PROSITE-ProRule annotation
Disulfide bondi1677 ↔ 1690PROSITE-ProRule annotation
Disulfide bondi1696 ↔ 1708PROSITE-ProRule annotation
Disulfide bondi1703 ↔ 1717PROSITE-ProRule annotation
Glycosylationi1714 – 17141N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1719 ↔ 1732PROSITE-ProRule annotation
Glycosylationi1745 – 17451N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1756 – 17561N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1812 ↔ 1824PROSITE-ProRule annotation
Disulfide bondi1819 ↔ 1833PROSITE-ProRule annotation
Disulfide bondi1835 ↔ 1848PROSITE-ProRule annotation
Disulfide bondi1854 ↔ 1867PROSITE-ProRule annotation
Disulfide bondi1861 ↔ 1876PROSITE-ProRule annotation
Disulfide bondi1878 ↔ 1890PROSITE-ProRule annotation
Disulfide bondi1896 ↔ 1908PROSITE-ProRule annotation
Disulfide bondi1903 ↔ 1917PROSITE-ProRule annotation
Disulfide bondi1919 ↔ 1932PROSITE-ProRule annotation
Disulfide bondi1938 ↔ 1948PROSITE-ProRule annotation
Disulfide bondi1943 ↔ 1957PROSITE-ProRule annotation
Glycosylationi1945 – 19451N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1959 ↔ 1971PROSITE-ProRule annotation
Disulfide bondi1977 ↔ 1990PROSITE-ProRule annotation
Disulfide bondi1985 ↔ 1999PROSITE-ProRule annotation
Disulfide bondi2001 ↔ 2014PROSITE-ProRule annotation
Disulfide bondi2020 ↔ 2032PROSITE-ProRule annotation
Disulfide bondi2027 ↔ 2041PROSITE-ProRule annotation
Disulfide bondi2043 ↔ 2054PROSITE-ProRule annotation
Disulfide bondi2060 ↔ 2072PROSITE-ProRule annotation
Disulfide bondi2067 ↔ 2081PROSITE-ProRule annotation
Disulfide bondi2083 ↔ 2096PROSITE-ProRule annotation
Glycosylationi2120 – 21201N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2175 ↔ 2187PROSITE-ProRule annotation
Disulfide bondi2182 ↔ 2196PROSITE-ProRule annotation
Disulfide bondi2198 ↔ 2211PROSITE-ProRule annotation
Disulfide bondi2217 ↔ 2228PROSITE-ProRule annotation
Disulfide bondi2223 ↔ 2237PROSITE-ProRule annotation
Glycosylationi2225 – 22251N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2239 ↔ 2251PROSITE-ProRule annotation
Disulfide bondi2257 ↔ 2268PROSITE-ProRule annotation
Disulfide bondi2264 ↔ 2277PROSITE-ProRule annotation
Disulfide bondi2279 ↔ 2292PROSITE-ProRule annotation
Disulfide bondi2298 ↔ 2312PROSITE-ProRule annotation
Disulfide bondi2305 ↔ 2321PROSITE-ProRule annotation
Disulfide bondi2323 ↔ 2336PROSITE-ProRule annotation
Disulfide bondi2342 ↔ 2354PROSITE-ProRule annotation
Disulfide bondi2349 ↔ 2363PROSITE-ProRule annotation
Disulfide bondi2365 ↔ 2378PROSITE-ProRule annotation
Disulfide bondi2453 ↔ 2465PROSITE-ProRule annotation
Disulfide bondi2460 ↔ 2474PROSITE-ProRule annotation
Disulfide bondi2476 ↔ 2489PROSITE-ProRule annotation
Disulfide bondi2495 ↔ 2506PROSITE-ProRule annotation
Disulfide bondi2502 ↔ 2515PROSITE-ProRule annotation
Disulfide bondi2517 ↔ 2530PROSITE-ProRule annotation
Disulfide bondi2536 ↔ 2547PROSITE-ProRule annotation
Disulfide bondi2543 ↔ 2556PROSITE-ProRule annotation
Disulfide bondi2558 ↔ 2569PROSITE-ProRule annotation
Disulfide bondi2575 ↔ 2588PROSITE-ProRule annotation
Disulfide bondi2582 ↔ 2597PROSITE-ProRule annotation
Disulfide bondi2599 ↔ 2612PROSITE-ProRule annotation
Disulfide bondi2618 ↔ 2628PROSITE-ProRule annotation
Disulfide bondi2624 ↔ 2637PROSITE-ProRule annotation
Disulfide bondi2639 ↔ 2652PROSITE-ProRule annotation
Disulfide bondi2658 ↔ 2669PROSITE-ProRule annotation
Disulfide bondi2664 ↔ 2678PROSITE-ProRule annotation
Disulfide bondi2680 ↔ 2693PROSITE-ProRule annotation
Disulfide bondi2699 ↔ 2710PROSITE-ProRule annotation
Disulfide bondi2706 ↔ 2719PROSITE-ProRule annotation
Disulfide bondi2721 ↔ 2733PROSITE-ProRule annotation
Glycosylationi2808 – 28081N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP35556.
PaxDbiP35556.
PRIDEiP35556.

PTM databases

PhosphoSiteiP35556.

Expressioni

Gene expression databases

BgeeiP35556.
CleanExiHS_FBN2.
ExpressionAtlasiP35556. baseline and differential.
GenevestigatoriP35556.

Organism-specific databases

HPAiCAB026401.
HPA012853.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
FBN1P355552EBI-6164392,EBI-2505934
FN1P027512EBI-6164392,EBI-1220319

Protein-protein interaction databases

BioGridi108495. 12 interactions.
IntActiP35556. 5 interactions.
STRINGi9606.ENSP00000262464.

Structurei

3D structure databases

ProteinModelPortaliP35556.
SMRiP35556. Positions 75-996, 1073-2326, 2338-2721.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini111 – 14232EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini145 – 17632EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini176 – 20833EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini214 – 26653TB 1Add
BLAST
Domaini276 – 31742EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini318 – 35942EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini364 – 41754TB 2Add
BLAST
Domaini494 – 53441EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini535 – 57440EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini575 – 61642EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini617 – 65741EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini658 – 69841EGF-like 10; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini704 – 75653TB 3Add
BLAST
Domaini768 – 80942EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini810 – 85142EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini852 – 89140EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini896 – 94752TB 4Add
BLAST
Domaini955 – 99642EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1001 – 105252TB 5Add
BLAST
Domaini1073 – 111442EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1115 – 115743EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1158 – 119942EGF-like 17; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1200 – 124142EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1242 – 128241EGF-like 19; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1283 – 132442EGF-like 20; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1325 – 136642EGF-like 21; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1367 – 140741EGF-like 22; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1408 – 144841EGF-like 23; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1449 – 149042EGF-like 24; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1491 – 153141EGF-like 25; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1532 – 157241EGF-like 26; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1577 – 163357TB 6Add
BLAST
Domaini1650 – 169142EGF-like 27; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1692 – 173342EGF-like 28; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1738 – 179154TB 7Add
BLAST
Domaini1808 – 184942EGF-like 29; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1850 – 189142EGF-like 30; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1892 – 193342EGF-like 31; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1934 – 197239EGF-like 32; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1973 – 201543EGF-like 33; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2016 – 205540EGF-like 34; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2056 – 209742EGF-like 35; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2102 – 215554TB 8Add
BLAST
Domaini2171 – 221242EGF-like 36; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2213 – 225240EGF-like 37; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2253 – 229341EGF-like 38; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2294 – 233744EGF-like 39; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2338 – 237942EGF-like 40; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2384 – 243754TB 9Add
BLAST
Domaini2449 – 249042EGF-like 41; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2491 – 253141EGF-like 42; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2532 – 257039EGF-like 43; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2571 – 261343EGF-like 44; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2614 – 265340EGF-like 45; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2654 – 269441EGF-like 46; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2695 – 273440EGF-like 47; calcium-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the fibrillin family.Curated
Contains 47 EGF-like domains.PROSITE-ProRule annotation
Contains 9 TB (TGF-beta binding) domains.Curated

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00750000117321.
HOGENOMiHOG000231768.
HOVERGENiHBG005643.
InParanoidiP35556.
OMAiSGRNCID.
OrthoDBiEOG7RV9F6.
PhylomeDBiP35556.
TreeFamiTF316849.

Family and domain databases

Gene3Di3.90.290.10. 9 hits.
InterProiIPR026823. cEGF.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR011398. FBN/EtMIC4.
IPR009030. Growth_fac_rcpt_N_dom.
IPR017878. TB_dom.
[Graphical view]
PANTHERiPTHR24039. PTHR24039. 1 hit.
PfamiPF12662. cEGF. 1 hit.
PF07645. EGF_CA. 41 hits.
PF00683. TB. 9 hits.
[Graphical view]
PIRSFiPIRSF036312. Fibrillin. 1 hit.
SMARTiSM00181. EGF. 3 hits.
SM00179. EGF_CA. 43 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 13 hits.
SSF57581. SSF57581. 9 hits.
PROSITEiPS00010. ASX_HYDROXYL. 43 hits.
PS00022. EGF_1. 2 hits.
PS01186. EGF_2. 37 hits.
PS50026. EGF_3. 45 hits.
PS01187. EGF_CA. 43 hits.
PS51364. TB. 9 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P35556-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGRRRRLCLQ LYFLWLGCVV LWAQGTAGQP QPPPPKPPRP QPPPQQVRSA
60 70 80 90 100
TAGSEGGFLA PEYREEGAAV ASRVRRRGQQ DVLRGPNVCG SRFHSYCCPG
110 120 130 140 150
WKTLPGGNQC IVPICRNSCG DGFCSRPNMC TCSSGQISST CGSKSIQQCS
160 170 180 190 200
VRCMNGGTCA DDHCQCQKGY IGTYCGQPVC ENGCQNGGRC IGPNRCACVY
210 220 230 240 250
GFTGPQCERD YRTGPCFTQV NNQMCQGQLT GIVCTKTLCC ATIGRAWGHP
260 270 280 290 300
CEMCPAQPQP CRRGFIPNIR TGACQDVDEC QAIPGICQGG NCINTVGSFE
310 320 330 340 350
CRCPAGHKQS ETTQKCEDID ECSIIPGICE TGECSNTVGS YFCVCPRGYV
360 370 380 390 400
TSTDGSRCID QRTGMCFSGL VNGRCAQELP GRMTKMQCCC EPGRCWGIGT
410 420 430 440 450
IPEACPVRGS EEYRRLCMDG LPMGGIPGSA GSRPGGTGGN GFAPSGNGNG
460 470 480 490 500
YGPGGTGFIP IPGGNGFSPG VGGAGVGAGG QGPIITGLTI LNQTIDICKH
510 520 530 540 550
HANLCLNGRC IPTVSSYRCE CNMGYKQDAN GDCIDVDECT SNPCTNGDCV
560 570 580 590 600
NTPGSYYCKC HAGFQRTPTK QACIDIDECI QNGVLCKNGR CVNTDGSFQC
610 620 630 640 650
ICNAGFELTT DGKNCVDHDE CTTTNMCLNG MCINEDGSFK CICKPGFVLA
660 670 680 690 700
PNGRYCTDVD ECQTPGICMN GHCINSEGSF RCDCPPGLAV GMDGRVCVDT
710 720 730 740 750
HMRSTCYGGI KKGVCVRPFP GAVTKSECCC ANPDYGFGEP CQPCPAKNSA
760 770 780 790 800
EFHGLCSSGV GITVDGRDIN ECALDPDICA NGICENLRGS YRCNCNSGYE
810 820 830 840 850
PDASGRNCID IDECLVNRLL CDNGLCRNTP GSYSCTCPPG YVFRTETETC
860 870 880 890 900
EDINECESNP CVNGACRNNL GSFNCECSPG SKLSSTGLIC IDSLKGTCWL
910 920 930 940 950
NIQDSRCEVN INGATLKSEC CATLGAAWGS PCERCELDTA CPRGLARIKG
960 970 980 990 1000
VTCEDVNECE VFPGVCPNGR CVNSKGSFHC ECPEGLTLDG TGRVCLDIRM
1010 1020 1030 1040 1050
EQCYLKWDED ECIHPVPGKF RMDACCCAVG AAWGTECEEC PKPGTKEYET
1060 1070 1080 1090 1100
LCPRGAGFAN RGDVLTGRPF YKDINECKAF PGMCTYGKCR NTIGSFKCRC
1110 1120 1130 1140 1150
NSGFALDMEE RNCTDIDECR ISPDLCGSGI CVNTPGSFEC ECFEGYESGF
1160 1170 1180 1190 1200
MMMKNCMDID ECERNPLLCR GGTCVNTEGS FQCDCPLGHE LSPSREDCVD
1210 1220 1230 1240 1250
INECSLSDNL CRNGKCVNMI GTYQCSCNPG YQATPDRQGC TDIDECMIMN
1260 1270 1280 1290 1300
GGCDTQCTNS EGSYECSCSE GYALMPDGRS CADIDECENN PDICDGGQCT
1310 1320 1330 1340 1350
NIPGEYRCLC YDGFMASMDM KTCIDVNECD LNSNICMFGE CENTKGSFIC
1360 1370 1380 1390 1400
HCQLGYSVKK GTTGCTDVDE CEIGAHNCDM HASCLNIPGS FKCSCREGWI
1410 1420 1430 1440 1450
GNGIKCIDLD ECSNGTHQCS INAQCVNTPG SYRCACSEGF TGDGFTCSDV
1460 1470 1480 1490 1500
DECAENINLC ENGQCLNVPG AYRCECEMGF TPASDSRSCQ DIDECSFQNI
1510 1520 1530 1540 1550
CVFGTCNNLP GMFHCICDDG YELDRTGGNC TDIDECADPI NCVNGLCVNT
1560 1570 1580 1590 1600
PGRYECNCPP DFQLNPTGVG CVDNRVGNCY LKFGPRGDGS LSCNTEIGVG
1610 1620 1630 1640 1650
VSRSSCCCSL GKAWGNPCET CPPVNSTEYY TLCPGGEGFR PNPITIILED
1660 1670 1680 1690 1700
IDECQELPGL CQGGNCINTF GSFQCECPQG YYLSEDTRIC EDIDECFAHP
1710 1720 1730 1740 1750
GVCGPGTCYN TLGNYTCICP PEYMQVNGGH NCMDMRKSFC YRSYNGTTCE
1760 1770 1780 1790 1800
NELPFNVTKR MCCCTYNVGK AWNKPCEPCP TPGTADFKTI CGNIPGFTFD
1810 1820 1830 1840 1850
IHTGKAVDID ECKEIPGICA NGVCINQIGS FRCECPTGFS YNDLLLVCED
1860 1870 1880 1890 1900
IDECSNGDNL CQRNADCINS PGSYRCECAA GFKLSPNGAC VDRNECLEIP
1910 1920 1930 1940 1950
NVCSHGLCVD LQGSYQCICH NGFKASQDQT MCMDVDECER HPCGNGTCKN
1960 1970 1980 1990 2000
TVGSYNCLCY PGFELTHNND CLDIDECSSF FGQVCRNGRC FNEIGSFKCL
2010 2020 2030 2040 2050
CNEGYELTPD GKNCIDTNEC VALPGSCSPG TCQNLEGSFR CICPPGYEVK
2060 2070 2080 2090 2100
SENCIDINEC DEDPNICLFG SCTNTPGGFQ CLCPPGFVLS DNGRRCFDTR
2110 2120 2130 2140 2150
QSFCFTNFEN GKCSVPKAFN TTKAKCCCSK MPGEGWGDPC ELCPKDDEVA
2160 2170 2180 2190 2200
FQDLCPYGHG TVPSLHDTRE DVNECLESPG ICSNGQCINT DGSFRCECPM
2210 2220 2230 2240 2250
GYNLDYTGVR CVDTDECSIG NPCGNGTCTN VIGSFECNCN EGFEPGPMMN
2260 2270 2280 2290 2300
CEDINECAQN PLLCAFRCMN TFGSYECTCP IGYALREDQK MCKDLDECAE
2310 2320 2330 2340 2350
GLHDCESRGM MCKNLIGTFM CICPPGMARR PDGEGCVDEN ECRTKPGICE
2360 2370 2380 2390 2400
NGRCVNIIGS YRCECNEGFQ SSSSGTECLD NRQGLCFAEV LQTICQMASS
2410 2420 2430 2440 2450
SRNLVTKSEC CCDGGRGWGH QCELCPLPGT AQYKKICPHG PGYTTDGRDI
2460 2470 2480 2490 2500
DECKVMPNLC TNGQCINTMG SFRCFCKVGY TTDISGTSCI DLDECSQSPK
2510 2520 2530 2540 2550
PCNYICKNTE GSYQCSCPRG YVLQEDGKTC KDLDECQTKQ HNCQFLCVNT
2560 2570 2580 2590 2600
LGGFTCKCPP GFTQHHTACI DNNECGSQPS LCGAKGICQN TPGSFSCECQ
2610 2620 2630 2640 2650
RGFSLDATGL NCEDVDECDG NHRCQHGCQN ILGGYRCGCP QGYIQHYQWN
2660 2670 2680 2690 2700
QCVDENECSN PNACGSASCY NTLGSYKCAC PSGFSFDQFS SACHDVNECS
2710 2720 2730 2740 2750
SSKNPCNYGC SNTEGGYLCG CPPGYYRVGQ GHCVSGMGFN KGQYLSLDTE
2760 2770 2780 2790 2800
VDEENALSPE ACYECKINGY SKKDSRQKRS IHEPDPTAVE QISLESVDMD
2810 2820 2830 2840 2850
SPVNMKFNLS HLGSKEHILE LRPAIQPLNN HIRYVISQGN DDSVFRIHQR
2860 2870 2880 2890 2900
NGLSYLHTAK KKLMPGTYTL EITSIPLYKK KELKKLEESN EDDYLLGELG
2910
EALRMRLQIQ LY
Length:2,912
Mass (Da):314,775
Last modified:May 26, 2009 - v3
Checksum:i0F0D78319E9911E6
GO
Isoform 2 (identifier: P35556-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     113-145: Missing.
     1491-1506: DIDECSFQNICVFGTC → GGSPGFQLIFKLDQPQ
     1507-2912: Missing.

Show »
Length:1,473
Mass (Da):157,690
Checksum:i2B6620CFCA6F7A72
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti146 – 1461I → L in BAG62163. (PubMed:14702039)Curated
Sequence conflicti192 – 1954GPNR → AQP in AAA18950. (PubMed:8120105)Curated
Sequence conflicti243 – 2431I → T in AAA18950. (PubMed:8120105)Curated
Sequence conflicti243 – 2431I → T in BAG62163. (PubMed:14702039)Curated
Sequence conflicti1161 – 11611E → G in AAA18950. (PubMed:8120105)Curated
Sequence conflicti1161 – 11611E → G in CAB56757. (PubMed:1852206)Curated
Sequence conflicti1244 – 12441D → G in BAG62163. (PubMed:14702039)Curated
Sequence conflicti1409 – 14091L → R in CAB56757. (PubMed:1852206)Curated
Sequence conflicti1503 – 15031F → S in AAA18950. (PubMed:8120105)Curated
Sequence conflicti2584 – 25841A → G in AAA18950. (PubMed:8120105)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti391 – 3911E → K in DA9.
VAR_015851
Natural varianti594 – 5941T → S.2 Publications
VAR_054979
Natural varianti681 – 6811R → H.1 Publication
VAR_054980
Natural varianti754 – 7541G → S in DA9. 1 Publication
VAR_058364
Natural varianti965 – 9651V → I.3 Publications
Corresponds to variant rs154001 [ dbSNP | Ensembl ].
VAR_002349
Natural varianti1057 – 10571G → D in DA9. 2 Publications
VAR_054981
Natural varianti1091 – 10911N → S in DA9. 1 Publication
VAR_058365
Natural varianti1093 – 10931I → T in DA9. 2 Publications
VAR_054982
Natural varianti1115 – 11151D → H in DA9; the underlying nucleotide substitution also causes low level in-frame mis-splicing of exon 25. 2 Publications
VAR_010739
Natural varianti1122 – 11221S → P in DA9. 1 Publication
VAR_058366
Natural varianti1142 – 11421C → F in DA9. 2 Publications
VAR_010740
Natural varianti1142 – 11421C → R in DA9. 1 Publication
VAR_058367
Natural varianti1146 – 11461Y → C in DA9. 1 Publication
VAR_058368
Natural varianti1156 – 11561C → F in DA9. 1 Publication
VAR_058369
Natural varianti1161 – 11611E → K in DA9. 1 Publication
VAR_058370
Natural varianti1179 – 11791G → C in DA9. 1 Publication
VAR_054983
Natural varianti1198 – 11981C → Y in DA9. 1 Publication
VAR_054984
Natural varianti1240 – 12401C → R in DA9. 1 Publication
VAR_054985
Natural varianti1246 – 12461C → F in DA9. 1 Publication
VAR_058371
Natural varianti1253 – 12531C → W in DA9. 2 Publications
Corresponds to variant rs28931602 [ dbSNP | Ensembl ].
VAR_010741
Natural varianti1253 – 12531C → Y in DA9. 2 Publications
VAR_002350
Natural varianti1257 – 12571C → W in DA9. 1 Publication
VAR_054986
Natural varianti1268 – 12681C → R in DA9. 1 Publication
VAR_054987
Natural varianti1384 – 13841C → F in DA9. 1 Publication
VAR_058372
Natural varianti1384 – 13841C → Y in DA9. 1 Publication
VAR_058373
Natural varianti1408 – 14081D → N in DA9. 1 Publication
VAR_058374
Natural varianti1425 – 14251C → R in DA9. 1 Publication
VAR_058375
Natural varianti1434 – 14341C → S in DA9. 2 Publications
VAR_002351
Natural varianti1772 – 17721W → G.2 Publications
VAR_054988
Natural varianti2062 – 20621E → V Found in a renal cell carcinoma case; somatic mutation. 1 Publication
VAR_064705
Natural varianti2266 – 22661F → L.2 Publications
VAR_054989
Natural varianti2278 – 22781T → M.
Corresponds to variant rs2307109 [ dbSNP | Ensembl ].
VAR_055415
Natural varianti2311 – 23111M → V.
Corresponds to variant rs32209 [ dbSNP | Ensembl ].
VAR_055416
Natural varianti2428 – 24281P → T.1 Publication
Corresponds to variant rs1801169 [ dbSNP | Ensembl ].
VAR_016143
Natural varianti2580 – 25801S → L.1 Publication
Corresponds to variant rs2291628 [ dbSNP | Ensembl ].
VAR_055417
Natural varianti2581 – 25811L → S.
Corresponds to variant rs2291628 [ dbSNP | Ensembl ].
VAR_054990
Natural varianti2771 – 27711S → P.2 Publications
Corresponds to variant rs1801170 [ dbSNP | Ensembl ].
VAR_014664

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei113 – 14533Missing in isoform 2. 2 PublicationsVSP_037369Add
BLAST
Alternative sequencei1491 – 150616DIDEC…VFGTC → GGSPGFQLIFKLDQPQ in isoform 2. 2 PublicationsVSP_037370Add
BLAST
Alternative sequencei1507 – 29121406Missing in isoform 2. 2 PublicationsVSP_037371Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U03272 mRNA. Translation: AAA18950.1.
AK300440 mRNA. Translation: BAG62163.1.
AC025169 Genomic DNA. No translation available.
AC034235 Genomic DNA. No translation available.
AC113387 Genomic DNA. No translation available.
X62009 mRNA. Translation: CAB56757.1.
AB209735 mRNA. Translation: BAD92972.1.
CCDSiCCDS34222.1. [P35556-1]
PIRiA54105.
RefSeqiNP_001990.2. NM_001999.3. [P35556-1]
UniGeneiHs.519294.

Genome annotation databases

EnsembliENST00000262464; ENSP00000262464; ENSG00000138829. [P35556-1]
ENST00000508053; ENSP00000424571; ENSG00000138829. [P35556-1]
GeneIDi2201.
KEGGihsa:2201.
UCSCiuc003kuu.3. human. [P35556-1]

Polymorphism databases

DMDMi238054385.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U03272 mRNA. Translation: AAA18950.1 .
AK300440 mRNA. Translation: BAG62163.1 .
AC025169 Genomic DNA. No translation available.
AC034235 Genomic DNA. No translation available.
AC113387 Genomic DNA. No translation available.
X62009 mRNA. Translation: CAB56757.1 .
AB209735 mRNA. Translation: BAD92972.1 .
CCDSi CCDS34222.1. [P35556-1 ]
PIRi A54105.
RefSeqi NP_001990.2. NM_001999.3. [P35556-1 ]
UniGenei Hs.519294.

3D structure databases

ProteinModelPortali P35556.
SMRi P35556. Positions 75-996, 1073-2326, 2338-2721.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108495. 12 interactions.
IntActi P35556. 5 interactions.
STRINGi 9606.ENSP00000262464.

PTM databases

PhosphoSitei P35556.

Polymorphism databases

DMDMi 238054385.

Proteomic databases

MaxQBi P35556.
PaxDbi P35556.
PRIDEi P35556.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262464 ; ENSP00000262464 ; ENSG00000138829 . [P35556-1 ]
ENST00000508053 ; ENSP00000424571 ; ENSG00000138829 . [P35556-1 ]
GeneIDi 2201.
KEGGi hsa:2201.
UCSCi uc003kuu.3. human. [P35556-1 ]

Organism-specific databases

CTDi 2201.
GeneCardsi GC05M127621.
GeneReviewsi FBN2.
H-InvDB HIX0005141.
HIX0137461.
HGNCi HGNC:3604. FBN2.
HPAi CAB026401.
HPA012853.
MIMi 121050. phenotype.
612570. gene.
neXtProti NX_P35556.
Orphaneti 115. Congenital contractural arachnodactyly.
PharmGKBi PA28017.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00750000117321.
HOGENOMi HOG000231768.
HOVERGENi HBG005643.
InParanoidi P35556.
OMAi SGRNCID.
OrthoDBi EOG7RV9F6.
PhylomeDBi P35556.
TreeFami TF316849.

Enzyme and pathway databases

Reactomei REACT_118572. Degradation of the extracellular matrix.
REACT_150331. Molecules associated with elastic fibres.
REACT_150366. Elastic fibre formation.

Miscellaneous databases

GenomeRNAii 2201.
NextBioi 8895.
PROi P35556.
SOURCEi Search...

Gene expression databases

Bgeei P35556.
CleanExi HS_FBN2.
ExpressionAtlasi P35556. baseline and differential.
Genevestigatori P35556.

Family and domain databases

Gene3Di 3.90.290.10. 9 hits.
InterProi IPR026823. cEGF.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR011398. FBN/EtMIC4.
IPR009030. Growth_fac_rcpt_N_dom.
IPR017878. TB_dom.
[Graphical view ]
PANTHERi PTHR24039. PTHR24039. 1 hit.
Pfami PF12662. cEGF. 1 hit.
PF07645. EGF_CA. 41 hits.
PF00683. TB. 9 hits.
[Graphical view ]
PIRSFi PIRSF036312. Fibrillin. 1 hit.
SMARTi SM00181. EGF. 3 hits.
SM00179. EGF_CA. 43 hits.
[Graphical view ]
SUPFAMi SSF57184. SSF57184. 13 hits.
SSF57581. SSF57581. 9 hits.
PROSITEi PS00010. ASX_HYDROXYL. 43 hits.
PS00022. EGF_1. 2 hits.
PS01186. EGF_2. 37 hits.
PS50026. EGF_3. 45 hits.
PS01187. EGF_CA. 43 hits.
PS51364. TB. 9 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and expression of fibrillin-2, a novel microfibrillar component preferentially located in elastic matrices."
    Zhang H., Apfelroth S.D., Hu W., Davis E.C., Sanguineti C., Bonadio J., Mecham R.P., Ramirez F.
    J. Cell Biol. 124:855-863(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS SER-594; GLY-1772; LEU-2266; LEU-2580 AND PRO-2771.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Placenta.
  3. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Linkage of Marfan syndrome and a phenotypically related disorder to two different fibrillin genes."
    Lee B., Godfrey M., Vitale E., Hori H., Mattei M.-G., Sarfarazi M., Tsipouras P., Ramirez F., Hollister D.W.
    Nature 352:330-334(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 752-2912 (ISOFORM 2).
  5. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 937-2912 (ISOFORM 1).
    Tissue: Aortic endothelium.
  6. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1112.
    Tissue: Liver.
  7. "Fibrillin-2 (FBN2) mutations result in the Marfan-like disorder, congenital contractural arachnodactyly."
    Putnam E.A., Zhang H., Ramirez F., Milewicz D.M.
    Nat. Genet. 11:456-458(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS DA9 TYR-1253 AND SER-1434, VARIANT ILE-965.
  8. "Clustering of FBN2 mutations in patients with congenital contractural arachnodactyly indicates an important role of the domains encoded by exons 24 through 34 during human development."
    Park E.-S., Putnam E.A., Chitayat D., Child A., Milewicz D.M.
    Am. J. Med. Genet. 78:350-355(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS DA9 ASP-1057 AND THR-1093, VARIANTS SER-594; HIS-681; ILE-965; GLY-1772; LEU-2266; THR-2428 AND PRO-2771.
  9. "A single mutation that results in an Asp-to-His substitution and partial exon skipping in a family with congenital contractural arachnodactyly."
    Babcock D., Gasner C., Francke U., Maslen C.
    Hum. Genet. 103:22-28(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT DA9 HIS-1115.
  10. "Two novel fibrillin-2 mutations in congenital contractural arachnodactyly."
    Belleh S., Zhou G., Wang M., Der Kaloustian V.M., Pagon R.A., Godfrey M.
    Am. J. Med. Genet. 92:7-12(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS DA9 PHE-1142 AND TRP-1253.
  11. "Ten novel FBN2 mutations in congenital contractural arachnodactyly: delineation of the molecular pathogenesis and clinical phenotype."
    Gupta P.A., Putnam E.A., Carmical S.G., Kaitila I., Steinmann B., Child A., Danesino C., Metcalfe K., Berry S.A., Chen E., Delorme C.V., Thong M.-K., Ades L.C., Milewicz D.M.
    Hum. Mutat. 19:39-48(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS DA9 ASP-1057; THR-1093; PHE-1142; CYS-1179; TYR-1198; ARG-1240; TRP-1253; TYR-1253; TRP-1257; ARG-1268 AND SER-1434, VARIANT ILE-965.
  12. "Comprehensive clinical and molecular assessment of 32 probands with congenital contractural arachnodactyly: report of 14 novel mutations and review of the literature."
    Callewaert B.L., Loeys B.L., Ficcadenti A., Vermeer S., Landgren M., Kroes H.Y., Yaron Y., Pope M., Foulds N., Boute O., Galan F., Kingston H., Van der Aa N., Salcedo I., Swinkels M.E., Wallgren-Pettersson C., Gabrielli O., De Backer J., Coucke P.J., De Paepe A.M.
    Hum. Mutat. 30:334-341(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS DA9 SER-754; SER-1091; HIS-1115; PRO-1122; ARG-1142; CYS-1146; PHE-1156; LYS-1161; PHE-1246; PHE-1384; TYR-1384; ASN-1408 AND ARG-1425.
  13. Cited for: VARIANT VAL-2062.

Entry informationi

Entry nameiFBN2_HUMAN
AccessioniPrimary (citable) accession number: P35556
Secondary accession number(s): B4DU01, Q59ES6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: May 26, 2009
Last modified: October 29, 2014
This is version 158 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

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